Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.11 (CD10)
 9,792 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

From rat brain, a membrane bound substance P-degrading endopeptidase (SPE) was purified 1580 fold to near homogeneity. After extraction with 10 mM CHAPS, the enzyme preparation was subjected to ion exchange chromatography on DEAE-cellulose, adsorption chromatography on hydroxyapatite, gelfiltration through Ultrogel AcA 44 and FPLC on Mono Q. This enzyme of 70,000 molecular weight is optimally active at pH 7.5. Metal chelators (EDTA and EGTA) and sulfhydryl modifying reagents (N-ethylmaleimide and p-chloromercuriphenylsulfonic acid) are strongly inhibitory while the serine-protease inhibitor diisopropyl-fluorophosphate does not effect the enzyme activity. The enzyme is strongly inhibited by bacitracin but not by phosphoramidon and captopril. Degradation of substance P is strongly inhibited by neurotensin, somatostatin, ACTH 1-39, and less effectively by LHRH but not by Leucine-enkephalin. Substance P is preferentially hydrolyzed at the Gln6-Phe7 peptide bond but fragmentation at the Pro4-Gln5, Gln5-Gln6,Phe7-Phe8 and Gly9-Leu10 bonds was also observed.
NIDA Res Monogr 1986
PMID:A membrane bound substance P degrading endopeptidase from rat brain. 244 28

Enkephalin had been shown to be almost exclusively hydrolyzed by three peptidases in the previous studies. In the present investigation, the relative importance of three enzymes in the inactivation of [Leu5]-enkephalin was examined in three isolated preparations. Results showed that amastatin-sensitive aminopeptidase played the greatest role in both guinea-pig ileum and rat vas deferens while it played the similar role to either phosphoramdidon-sensitive endopeptidase-24.11 or captopril-sensitive peptidyl dipeptidase A in mouse vas deferens.
NIDA Res Monogr 1986
PMID:Inactivation of [Leu5]-enkephalin in three isolated preparations: relative importance of aminopeptidase, endopeptidase-24.11 and peptidyl dipeptidase A. 282 76

An endopeptidase hydrolyzing dynorphins A and B and alpha-neo-endorphin at the Arg6-Arg7 or Arg6-Lys7 bonds, was partially purified from human cerebrospinal fluid and further characterized by various biochemical techniques including HPLC gel permeation (UltroPac TSK G3000SW) and ion exchange (TSK DEAE-3SW) chromatography. A procedure for quantitative analysis of the enzyme in individual CSF samples is also described. The activity in lumbar CSF of women in late pregnancy was significantly lower than that in control samples.
NIDA Res Monogr 1986
PMID:Assay and biochemical characterization of a dynorphin converting enzyme in human cerebrospinal fluid. 289 68

The tripeptide Tyr-Gly-Gly (YGG) was established as an endogenous constituent in rat brain. Its origin from enkephalin neurons is suggested by its regional distribution paralleling that of (Met5)-enkephalin (YGGFM), its decrease following kainate-induced ablation of the striato-pallidal neurons and its enhanced formation following depolarization of pallidal slices. Enkephalinase (EC 3.4.24.11) is selectively responsible for endogenous YGG formation in vitro and in vivo.
NIDA Res Monogr 1986
PMID:The endogenous tripeptide Tyr-Gly-Gly as an extracellular metabolite of enkephalins in rat brain: origin and metabolism. 312 44